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| | <StructureSection load='6k0l' size='340' side='right'caption='[[6k0l]], [[Resolution|resolution]] 1.58Å' scene=''> | | <StructureSection load='6k0l' size='340' side='right'caption='[[6k0l]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k0l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/African_green_monkey African green monkey]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K0L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k0l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorocebus_aethiops Chlorocebus aethiops]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K0L FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD163, M130 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9534 African green monkey])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6k0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k0l OCA], [https://pdbe.org/6k0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k0l RCSB], [https://www.ebi.ac.uk/pdbsum/6k0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k0l ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6k0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k0l OCA], [https://pdbe.org/6k0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k0l RCSB], [https://www.ebi.ac.uk/pdbsum/6k0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k0l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/C163A_CHLAE C163A_CHLAE]] Involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1 (By similarity). After shedding, the soluble form (sCD163) may play an anti-inflammatory role.
| + | [https://www.uniprot.org/uniprot/C163A_CHLAE C163A_CHLAE] Involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1 (By similarity). After shedding, the soluble form (sCD163) may play an anti-inflammatory role. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: African green monkey]] | + | [[Category: Chlorocebus aethiops]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jiang, L]] | + | [[Category: Jiang L]] |
| - | [[Category: Li, R]] | + | [[Category: Li R]] |
| - | [[Category: Ma, H]] | + | [[Category: Ma H]] |
| - | [[Category: Qiao, S]] | + | [[Category: Qiao S]] |
| - | [[Category: Zhang, G]] | + | [[Category: Zhang G]] |
| - | [[Category: Endocytosis]]
| + | |
| - | [[Category: Porcine reproductive and respiratory syndrome virus]]
| + | |
| - | [[Category: Scavenger receptor]]
| + | |
| - | [[Category: Scavenger receptor cysteine-rich domain]]
| + | |
| Structural highlights
Function
C163A_CHLAE Involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1 (By similarity). After shedding, the soluble form (sCD163) may play an anti-inflammatory role.
Publication Abstract from PubMed
Porcine reproductive and respiratory syndrome (PRRS) is a serious disease burdening global swine industry. Infection by its etiological agent, PRRS virus (PRRSV), shows a highly restricted tropism of host cells and has been demonstrated to be mediated by an essential scavenger receptor (SR) CD163. CD163 fifth SR cysteine-rich domain (SRCR5) is further proven to play a crucial role during viral infection. Despite intense research, the involvement of CD163 SRCR5 in PRRSV infection remains to be elucidated. In the current study, we prepared recombinant monkey CD163 (moCD163) SRCR5 and human CD163-like homolog (hCD163L1) SRCR8, and determined their crystal structures. After comparison with the previously reported crystal structure of porcine CD163 (pCD163) SRCR5, these structures showed almost identical structural folds but significantly different surface electrostatic potentials. Based on these differences, we carried out mutational research to identify that the charged residue at position 534 in association with the one at position 561 were important for PRRSV-2 infection in vitro. Altogether the current work sheds some light on CD163-mediated PRRSV-2 infection and deepens our understanding of the viral pathogenesis, which will provide clues for prevention and control of PRRS.
Structural comparison of CD163 SRCR5 from different species sheds some light on its involvement in porcine reproductive and respiratory syndrome virus-2 infection in vitro.,Ma H, Li R, Jiang L, Qiao S, Chen XX, Wang A, Zhang G Vet Res. 2021 Jun 30;52(1):97. doi: 10.1186/s13567-021-00969-z. PMID:34193250[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ma H, Li R, Jiang L, Qiao S, Chen XX, Wang A, Zhang G. Structural comparison of CD163 SRCR5 from different species sheds some light on its involvement in porcine reproductive and respiratory syndrome virus-2 infection in vitro. Vet Res. 2021 Jun 30;52(1):97. doi: 10.1186/s13567-021-00969-z. PMID:34193250 doi:http://dx.doi.org/10.1186/s13567-021-00969-z
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